View source for 6nqo


==Crystal structure of fast switching M159T mutant of fluorescent protein Dronpa (Dronpa2), Y63(3-IY)==
<StructureSection load='6nqo' size='340' side='right'caption='[[6nqo]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6nqo]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Echinophyllia_sp._SC22 Echinophyllia sp. SC22]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NQO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6NQO FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=KZG:{(4Z)-2-[(1R)-1-amino-2-sulfanylethyl]-4-[(4-hydroxy-3-iodophenyl)methylidene]-5-oxo-4,5-dihydro-1H-imidazol-1-yl}aceti+c+acid'>KZG</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6nqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nqo OCA], [https://pdbe.org/6nqo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6nqo RCSB], [https://www.ebi.ac.uk/pdbsum/6nqo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6nqo ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q5TLG6_9CNID Q5TLG6_9CNID] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Rotation around a specific bond after photoexcitation is central to vision and emerging opportunities in optogenetics, super-resolution microscopy, and photoactive molecular devices. Competing roles for steric and electrostatic effects that govern bond-specific photoisomerization have been widely discussed, the latter originating from chromophore charge transfer upon excitation. We systematically altered the electrostatic properties of the green fluorescent protein chromophore in a photoswitchable variant, Dronpa2, using amber suppression to introduce electron-donating and electron-withdrawing groups to the phenolate ring. Through analysis of the absorption (color), fluorescence quantum yield, and energy barriers to ground- and excited-state isomerization, we evaluate the contributions of sterics and electrostatics quantitatively and demonstrate how electrostatic effects bias the pathway of chromophore photoisomerization, leading to a generalized framework to guide protein design.

Electrostatic control of photoisomerization pathways in proteins.,Romei MG, Lin CY, Mathews II, Boxer SG Science. 2020 Jan 3;367(6473):76-79. doi: 10.1126/science.aax1898. PMID:31896714<ref>PMID:31896714</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6nqo" style="background-color:#fffaf0;"></div>

==See Also==
*[[Dronpa|Dronpa]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Echinophyllia sp. SC22]]
[[Category: Large Structures]]
[[Category: Boxer SG]]
[[Category: Lin C-Y]]
[[Category: Mathews II]]
[[Category: Romei MG]]